AMYGNN: A Graph Convolutional Neural Network-Based Approach for Predicting Amyloid Formation from Polypeptides

There has been an increasing interest in the use of amyloids for constructing various functional materials. The design of amyloid-associated functional materials requires the identification of the core peptide sequences as the fundamental building block. The existing computational methods are limited in terms of delineating polypeptides, the typical non-Euclidean structural data, and they fail to capture the dynamic interactions between amino acids due to ignoring the contextual information from surrounding amino acids. Here, we first propose the use of a state-of-the-art graph convolutional neural network for predicting the trends of amyloid formation from specific peptide sequences (AMYGNN) by abstracting each polypeptide as a graph, in which the constituting amino acids are viewed as nodes and edges characterizing the connections between pairs of amino acids are established when they meet a given distance threshold (C_α-C_α ≤ 5 Å). Our model achieves high performance with accuracy (0.9208), G-mean (0.9203), MCC (0.8417), and F1 (0.9235) in determining the characteristic peptide sequences to form amyloid. 32 of 534 crucial amino acid properties that greatly contribute to the formation of amyloids are ascertained, and the β-folding-like graph structure of a polypeptide is believed to be essential for the formation of amyloid. Our model enables the mapping of polypeptides with underlying interactions between amino acids and provides a quick and precise predictive framework for directing the construction of amyloid-associated functional materials.